Orthogonal coiled coils enable rapid covalent labelling of two distinct membrane proteins with peptide nucleic acid barcodes
RSC Chemical Biology, ISSN: 2633-0679, Vol: 2, Issue: 4, Page: 1291-1295
2021
- 5Citations
- 8Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations5
- Citation Indexes5
- CrossRef4
- Captures8
- Readers8
Article Description
Templated chemistry offers the prospect of addressing specificity challenges occurring in bioconjugation reactions. Here, we show two peptide-templated amide-bond forming reactions that enable the concurrent labelling of two different membrane proteins with two different peptide nucleic acid (PNA) barcodes. The reaction system is based on the mutually selective coiled coil interaction between two thioester-linked PNA-peptide conjugates and two cysteine peptides serving as genetically encoded peptide tags. Orthogonal coiled coil templated covalent labelling is highly specific, quantitative and proceeds within a minute. To demonstrate the usefulness, we evaluated receptor internalisation of two membranous receptors EGFR (epidermal growth factor) and ErbB2 (epidermal growth factor receptor 2) by first staining PNA-tagged proteins with fluorophore-DNA conjugates and then erasing signals from non-internalized receptors via toehold-mediated strand displacement. This journal is
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85112242314&origin=inward; http://dx.doi.org/10.1039/d1cb00126d; http://www.ncbi.nlm.nih.gov/pubmed/34458843; https://xlink.rsc.org/?DOI=D1CB00126D; https://dx.doi.org/10.1039/d1cb00126d; https://pubs.rsc.org/en/content/articlelanding/2021/cb/d1cb00126d
Royal Society of Chemistry (RSC)
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